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P35556

- FBN2_HUMAN

UniProt

P35556 - FBN2_HUMAN

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Protein

Fibrillin-2

Gene
FBN2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Fibrillins are structural components of 10-12 nm extracellular calcium-binding microfibrils, which occur either in association with elastin or in elastin-free bundles. Fibrillin-2-containing microfibrils regulate the early process of elastic fiber assembly. Regulates osteoblast maturation by controlling TGF-beta bioavailability and calibrating TGF-beta and BMP levels, respectively By similarity.

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. extracellular matrix structural constituent Source: ProtInc

GO - Biological processi

  1. anatomical structure morphogenesis Source: ProtInc
  2. bone trabecula formation Source: BHF-UCL
  3. embryonic limb morphogenesis Source: Ensembl
  4. extracellular matrix disassembly Source: Reactome
  5. extracellular matrix organization Source: Reactome
  6. positive regulation of bone mineralization Source: BHF-UCL
  7. positive regulation of osteoblast differentiation Source: BHF-UCL
  8. sequestering of TGFbeta in extracellular matrix Source: BHF-UCL
Complete GO annotation...

Keywords - Ligandi

Calcium

Enzyme and pathway databases

ReactomeiREACT_118572. Degradation of the extracellular matrix.
REACT_150331. Molecules associated with elastic fibres.
REACT_150366. Elastic fibre formation.

Names & Taxonomyi

Protein namesi
Recommended name:
Fibrillin-2
Gene namesi
Name:FBN2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:3604. FBN2.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: Reactome
  2. microfibril Source: BHF-UCL
  3. proteinaceous extracellular matrix Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Arthrogryposis, distal, 9 (DA9) [MIM:121050]: A form of distal arthrogryposis, a disease characterized by congenital joint contractures that mainly involve two or more distal parts of the limbs, in the absence of a primary neurological or muscle disease. DA9 is a connective tissue disorder characterized by contractures, arachnodactyly, scoliosis, and crumpled ears.
Note: The disease is caused by mutations affecting the gene represented in this entry.6 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti391 – 3911E → K in DA9.
VAR_015851
Natural varianti754 – 7541G → S in DA9. 1 Publication
VAR_058364
Natural varianti1057 – 10571G → D in DA9. 2 Publications
VAR_054981
Natural varianti1091 – 10911N → S in DA9. 1 Publication
VAR_058365
Natural varianti1093 – 10931I → T in DA9. 2 Publications
VAR_054982
Natural varianti1115 – 11151D → H in DA9; the underlying nucleotide substitution also causes low level in-frame mis-splicing of exon 25. 2 Publications
VAR_010739
Natural varianti1122 – 11221S → P in DA9. 1 Publication
VAR_058366
Natural varianti1142 – 11421C → F in DA9. 2 Publications
VAR_010740
Natural varianti1142 – 11421C → R in DA9. 1 Publication
VAR_058367
Natural varianti1146 – 11461Y → C in DA9. 1 Publication
VAR_058368
Natural varianti1156 – 11561C → F in DA9. 1 Publication
VAR_058369
Natural varianti1161 – 11611E → K in DA9. 1 Publication
VAR_058370
Natural varianti1179 – 11791G → C in DA9. 1 Publication
VAR_054983
Natural varianti1198 – 11981C → Y in DA9. 1 Publication
VAR_054984
Natural varianti1240 – 12401C → R in DA9. 1 Publication
VAR_054985
Natural varianti1246 – 12461C → F in DA9. 1 Publication
VAR_058371
Natural varianti1253 – 12531C → W in DA9. 2 Publications
Corresponds to variant rs28931602 [ dbSNP | Ensembl ].
VAR_010741
Natural varianti1253 – 12531C → Y in DA9. 2 Publications
VAR_002350
Natural varianti1257 – 12571C → W in DA9. 1 Publication
VAR_054986
Natural varianti1268 – 12681C → R in DA9. 1 Publication
VAR_054987
Natural varianti1384 – 13841C → F in DA9. 1 Publication
VAR_058372
Natural varianti1384 – 13841C → Y in DA9. 1 Publication
VAR_058373
Natural varianti1408 – 14081D → N in DA9. 1 Publication
VAR_058374
Natural varianti1425 – 14251C → R in DA9. 1 Publication
VAR_058375
Natural varianti1434 – 14341C → S in DA9. 2 Publications
VAR_002351

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi121050. phenotype.
Orphaneti115. Congenital contractural arachnodactyly.
PharmGKBiPA28017.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828 Reviewed predictionAdd
BLAST
Chaini29 – 29122884Fibrillin-2PRO_0000007584Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi115 ↔ 124 By similarity
Disulfide bondi119 ↔ 130 By similarity
Disulfide bondi132 ↔ 141 By similarity
Disulfide bondi149 ↔ 159 By similarity
Disulfide bondi153 ↔ 164 By similarity
Disulfide bondi166 ↔ 175 By similarity
Disulfide bondi180 ↔ 190 By similarity
Disulfide bondi184 ↔ 196 By similarity
Disulfide bondi198 ↔ 207 By similarity
Disulfide bondi280 ↔ 292 By similarity
Disulfide bondi287 ↔ 301 By similarity
Disulfide bondi303 ↔ 316 By similarity
Disulfide bondi322 ↔ 334 By similarity
Disulfide bondi329 ↔ 343 By similarity
Disulfide bondi345 ↔ 358 By similarity
Glycosylationi492 – 4921N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi498 ↔ 510 By similarity
Disulfide bondi505 ↔ 519 By similarity
Disulfide bondi521 ↔ 533 By similarity
Disulfide bondi539 ↔ 549 By similarity
Disulfide bondi544 ↔ 558 By similarity
Disulfide bondi560 ↔ 573 By similarity
Disulfide bondi579 ↔ 591 By similarity
Disulfide bondi586 ↔ 600 By similarity
Disulfide bondi602 ↔ 615 By similarity
Disulfide bondi621 ↔ 632 By similarity
Disulfide bondi627 ↔ 641 By similarity
Disulfide bondi643 ↔ 656 By similarity
Disulfide bondi662 ↔ 673 By similarity
Disulfide bondi668 ↔ 682 By similarity
Disulfide bondi684 ↔ 697 By similarity
Disulfide bondi772 ↔ 784 By similarity
Disulfide bondi779 ↔ 793 By similarity
Disulfide bondi795 ↔ 808 By similarity
Disulfide bondi814 ↔ 826 By similarity
Disulfide bondi821 ↔ 835 By similarity
Disulfide bondi837 ↔ 850 By similarity
Disulfide bondi856 ↔ 866 By similarity
Disulfide bondi861 ↔ 875 By similarity
Disulfide bondi877 ↔ 890 By similarity
Disulfide bondi959 ↔ 971 By similarity
Disulfide bondi966 ↔ 980 By similarity
Disulfide bondi982 ↔ 995 By similarity
Disulfide bondi1077 ↔ 1089 By similarity
Disulfide bondi1084 ↔ 1098 By similarity
Disulfide bondi1100 ↔ 1113 By similarity
Glycosylationi1112 – 11121N-linked (GlcNAc...)1 Publication
Disulfide bondi1119 ↔ 1131 By similarity
Disulfide bondi1126 ↔ 1140 By similarity
Disulfide bondi1142 ↔ 1156 By similarity
Disulfide bondi1162 ↔ 1174 By similarity
Disulfide bondi1169 ↔ 1183 By similarity
Disulfide bondi1185 ↔ 1198 By similarity
Disulfide bondi1204 ↔ 1216 By similarity
Disulfide bondi1211 ↔ 1225 By similarity
Disulfide bondi1227 ↔ 1240 By similarity
Disulfide bondi1246 ↔ 1257 By similarity
Disulfide bondi1253 ↔ 1266 By similarity
Disulfide bondi1268 ↔ 1281 By similarity
Disulfide bondi1287 ↔ 1299 By similarity
Disulfide bondi1294 ↔ 1308 By similarity
Disulfide bondi1310 ↔ 1323 By similarity
Disulfide bondi1329 ↔ 1341 By similarity
Disulfide bondi1336 ↔ 1350 By similarity
Disulfide bondi1352 ↔ 1365 By similarity
Disulfide bondi1371 ↔ 1384 By similarity
Disulfide bondi1378 ↔ 1393 By similarity
Disulfide bondi1395 ↔ 1406 By similarity
Disulfide bondi1412 ↔ 1425 By similarity
Glycosylationi1414 – 14141N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1419 ↔ 1434 By similarity
Disulfide bondi1436 ↔ 1447 By similarity
Disulfide bondi1453 ↔ 1465 By similarity
Disulfide bondi1460 ↔ 1474 By similarity
Disulfide bondi1476 ↔ 1489 By similarity
Disulfide bondi1495 ↔ 1506 By similarity
Disulfide bondi1501 ↔ 1515 By similarity
Disulfide bondi1517 ↔ 1530 By similarity
Glycosylationi1529 – 15291N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1536 ↔ 1547 By similarity
Disulfide bondi1542 ↔ 1556 By similarity
Disulfide bondi1558 ↔ 1571 By similarity
Glycosylationi1625 – 16251N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1654 ↔ 1666 By similarity
Disulfide bondi1661 ↔ 1675 By similarity
Disulfide bondi1677 ↔ 1690 By similarity
Disulfide bondi1696 ↔ 1708 By similarity
Disulfide bondi1703 ↔ 1717 By similarity
Glycosylationi1714 – 17141N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1719 ↔ 1732 By similarity
Glycosylationi1745 – 17451N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1756 – 17561N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1812 ↔ 1824 By similarity
Disulfide bondi1819 ↔ 1833 By similarity
Disulfide bondi1835 ↔ 1848 By similarity
Disulfide bondi1854 ↔ 1867 By similarity
Disulfide bondi1861 ↔ 1876 By similarity
Disulfide bondi1878 ↔ 1890 By similarity
Disulfide bondi1896 ↔ 1908 By similarity
Disulfide bondi1903 ↔ 1917 By similarity
Disulfide bondi1919 ↔ 1932 By similarity
Disulfide bondi1938 ↔ 1948 By similarity
Disulfide bondi1943 ↔ 1957 By similarity
Glycosylationi1945 – 19451N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1959 ↔ 1971 By similarity
Disulfide bondi1977 ↔ 1990 By similarity
Disulfide bondi1985 ↔ 1999 By similarity
Disulfide bondi2001 ↔ 2014 By similarity
Disulfide bondi2020 ↔ 2032 By similarity
Disulfide bondi2027 ↔ 2041 By similarity
Disulfide bondi2043 ↔ 2054 By similarity
Disulfide bondi2060 ↔ 2072 By similarity
Disulfide bondi2067 ↔ 2081 By similarity
Disulfide bondi2083 ↔ 2096 By similarity
Glycosylationi2120 – 21201N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2175 ↔ 2187 By similarity
Disulfide bondi2182 ↔ 2196 By similarity
Disulfide bondi2198 ↔ 2211 By similarity
Disulfide bondi2217 ↔ 2228 By similarity
Disulfide bondi2223 ↔ 2237 By similarity
Glycosylationi2225 – 22251N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2239 ↔ 2251 By similarity
Disulfide bondi2257 ↔ 2268 By similarity
Disulfide bondi2264 ↔ 2277 By similarity
Disulfide bondi2279 ↔ 2292 By similarity
Disulfide bondi2298 ↔ 2312 By similarity
Disulfide bondi2305 ↔ 2321 By similarity
Disulfide bondi2323 ↔ 2336 By similarity
Disulfide bondi2342 ↔ 2354 By similarity
Disulfide bondi2349 ↔ 2363 By similarity
Disulfide bondi2365 ↔ 2378 By similarity
Disulfide bondi2453 ↔ 2465 By similarity
Disulfide bondi2460 ↔ 2474 By similarity
Disulfide bondi2476 ↔ 2489 By similarity
Disulfide bondi2495 ↔ 2506 By similarity
Disulfide bondi2502 ↔ 2515 By similarity
Disulfide bondi2517 ↔ 2530 By similarity
Disulfide bondi2536 ↔ 2547 By similarity
Disulfide bondi2543 ↔ 2556 By similarity
Disulfide bondi2558 ↔ 2569 By similarity
Disulfide bondi2575 ↔ 2588 By similarity
Disulfide bondi2582 ↔ 2597 By similarity
Disulfide bondi2599 ↔ 2612 By similarity
Disulfide bondi2618 ↔ 2628 By similarity
Disulfide bondi2624 ↔ 2637 By similarity
Disulfide bondi2639 ↔ 2652 By similarity
Disulfide bondi2658 ↔ 2669 By similarity
Disulfide bondi2664 ↔ 2678 By similarity
Disulfide bondi2680 ↔ 2693 By similarity
Disulfide bondi2699 ↔ 2710 By similarity
Disulfide bondi2706 ↔ 2719 By similarity
Disulfide bondi2721 ↔ 2733 By similarity
Glycosylationi2808 – 28081N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP35556.
PaxDbiP35556.
PRIDEiP35556.

PTM databases

PhosphoSiteiP35556.

Expressioni

Gene expression databases

ArrayExpressiP35556.
BgeeiP35556.
CleanExiHS_FBN2.
GenevestigatoriP35556.

Organism-specific databases

HPAiCAB026401.
HPA012853.

Interactioni

Protein-protein interaction databases

BioGridi108495. 7 interactions.
IntActiP35556. 3 interactions.
STRINGi9606.ENSP00000262464.

Structurei

3D structure databases

ProteinModelPortaliP35556.
SMRiP35556. Positions 75-996, 1073-2330, 2338-2721.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini111 – 14232EGF-like 1Add
BLAST
Domaini145 – 17632EGF-like 2Add
BLAST
Domaini176 – 20833EGF-like 3Add
BLAST
Domaini214 – 26653TB 1Add
BLAST
Domaini276 – 31742EGF-like 4; calcium-bindingAdd
BLAST
Domaini318 – 35942EGF-like 5; calcium-bindingAdd
BLAST
Domaini364 – 41754TB 2Add
BLAST
Domaini494 – 53441EGF-like 6Add
BLAST
Domaini535 – 57440EGF-like 7; calcium-bindingAdd
BLAST
Domaini575 – 61642EGF-like 8; calcium-bindingAdd
BLAST
Domaini617 – 65741EGF-like 9; calcium-bindingAdd
BLAST
Domaini658 – 69841EGF-like 10; calcium-bindingAdd
BLAST
Domaini704 – 75653TB 3Add
BLAST
Domaini768 – 80942EGF-like 11; calcium-bindingAdd
BLAST
Domaini810 – 85142EGF-like 12; calcium-bindingAdd
BLAST
Domaini852 – 89140EGF-like 13; calcium-bindingAdd
BLAST
Domaini896 – 94752TB 4Add
BLAST
Domaini955 – 99642EGF-like 14; calcium-bindingAdd
BLAST
Domaini1001 – 105252TB 5Add
BLAST
Domaini1073 – 111442EGF-like 15; calcium-bindingAdd
BLAST
Domaini1115 – 115743EGF-like 16; calcium-bindingAdd
BLAST
Domaini1158 – 119942EGF-like 17; calcium-bindingAdd
BLAST
Domaini1200 – 124142EGF-like 18; calcium-bindingAdd
BLAST
Domaini1242 – 128241EGF-like 19; calcium-bindingAdd
BLAST
Domaini1283 – 132442EGF-like 20; calcium-bindingAdd
BLAST
Domaini1325 – 136642EGF-like 21; calcium-bindingAdd
BLAST
Domaini1367 – 140741EGF-like 22; calcium-bindingAdd
BLAST
Domaini1408 – 144841EGF-like 23; calcium-bindingAdd
BLAST
Domaini1449 – 149042EGF-like 24; calcium-bindingAdd
BLAST
Domaini1491 – 153141EGF-like 25; calcium-bindingAdd
BLAST
Domaini1532 – 157241EGF-like 26; calcium-bindingAdd
BLAST
Domaini1577 – 163357TB 6Add
BLAST
Domaini1650 – 169142EGF-like 27; calcium-bindingAdd
BLAST
Domaini1692 – 173342EGF-like 28; calcium-bindingAdd
BLAST
Domaini1738 – 179154TB 7Add
BLAST
Domaini1808 – 184942EGF-like 29; calcium-bindingAdd
BLAST
Domaini1850 – 189142EGF-like 30; calcium-bindingAdd
BLAST
Domaini1892 – 193342EGF-like 31; calcium-bindingAdd
BLAST
Domaini1934 – 197239EGF-like 32; calcium-bindingAdd
BLAST
Domaini1973 – 201543EGF-like 33; calcium-bindingAdd
BLAST
Domaini2016 – 205540EGF-like 34; calcium-bindingAdd
BLAST
Domaini2056 – 209742EGF-like 35; calcium-bindingAdd
BLAST
Domaini2102 – 215554TB 8Add
BLAST
Domaini2171 – 221242EGF-like 36; calcium-bindingAdd
BLAST
Domaini2213 – 225240EGF-like 37; calcium-bindingAdd
BLAST
Domaini2253 – 229341EGF-like 38; calcium-bindingAdd
BLAST
Domaini2294 – 233744EGF-like 39; calcium-bindingAdd
BLAST
Domaini2338 – 237942EGF-like 40; calcium-bindingAdd
BLAST
Domaini2384 – 243754TB 9Add
BLAST
Domaini2449 – 249042EGF-like 41; calcium-bindingAdd
BLAST
Domaini2491 – 253141EGF-like 42; calcium-bindingAdd
BLAST
Domaini2532 – 257039EGF-like 43; calcium-bindingAdd
BLAST
Domaini2571 – 261343EGF-like 44; calcium-bindingAdd
BLAST
Domaini2614 – 265340EGF-like 45; calcium-bindingAdd
BLAST
Domaini2654 – 269441EGF-like 46; calcium-bindingAdd
BLAST
Domaini2695 – 273440EGF-like 47; calcium-bindingAdd
BLAST

Sequence similaritiesi

Belongs to the fibrillin family.
Contains 47 EGF-like domains.

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiNOG12793.
HOGENOMiHOG000231768.
HOVERGENiHBG005643.
InParanoidiP35556.
OMAiSGRNCID.
OrthoDBiEOG7RV9F6.
PhylomeDBiP35556.
TreeFamiTF316849.

Family and domain databases

Gene3Di3.90.290.10. 9 hits.
InterProiIPR026823. cEGF.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR011398. FBN/EtMIC4.
IPR009030. Growth_fac_rcpt_N_dom.
IPR017878. TB_dom.
[Graphical view]
PANTHERiPTHR24039. PTHR24039. 1 hit.
PfamiPF12662. cEGF. 1 hit.
PF07645. EGF_CA. 41 hits.
PF00683. TB. 9 hits.
[Graphical view]
PIRSFiPIRSF036312. Fibrillin. 1 hit.
SMARTiSM00181. EGF. 3 hits.
SM00179. EGF_CA. 43 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 13 hits.
SSF57581. SSF57581. 9 hits.
PROSITEiPS00010. ASX_HYDROXYL. 43 hits.
PS00022. EGF_1. 2 hits.
PS01186. EGF_2. 37 hits.
PS50026. EGF_3. 45 hits.
PS01187. EGF_CA. 43 hits.
PS51364. TB. 9 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P35556-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

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MGRRRRLCLQ LYFLWLGCVV LWAQGTAGQP QPPPPKPPRP QPPPQQVRSA     50
TAGSEGGFLA PEYREEGAAV ASRVRRRGQQ DVLRGPNVCG SRFHSYCCPG 100
WKTLPGGNQC IVPICRNSCG DGFCSRPNMC TCSSGQISST CGSKSIQQCS 150
VRCMNGGTCA DDHCQCQKGY IGTYCGQPVC ENGCQNGGRC IGPNRCACVY 200
GFTGPQCERD YRTGPCFTQV NNQMCQGQLT GIVCTKTLCC ATIGRAWGHP 250
CEMCPAQPQP CRRGFIPNIR TGACQDVDEC QAIPGICQGG NCINTVGSFE 300
CRCPAGHKQS ETTQKCEDID ECSIIPGICE TGECSNTVGS YFCVCPRGYV 350
TSTDGSRCID QRTGMCFSGL VNGRCAQELP GRMTKMQCCC EPGRCWGIGT 400
IPEACPVRGS EEYRRLCMDG LPMGGIPGSA GSRPGGTGGN GFAPSGNGNG 450
YGPGGTGFIP IPGGNGFSPG VGGAGVGAGG QGPIITGLTI LNQTIDICKH 500
HANLCLNGRC IPTVSSYRCE CNMGYKQDAN GDCIDVDECT SNPCTNGDCV 550
NTPGSYYCKC HAGFQRTPTK QACIDIDECI QNGVLCKNGR CVNTDGSFQC 600
ICNAGFELTT DGKNCVDHDE CTTTNMCLNG MCINEDGSFK CICKPGFVLA 650
PNGRYCTDVD ECQTPGICMN GHCINSEGSF RCDCPPGLAV GMDGRVCVDT 700
HMRSTCYGGI KKGVCVRPFP GAVTKSECCC ANPDYGFGEP CQPCPAKNSA 750
EFHGLCSSGV GITVDGRDIN ECALDPDICA NGICENLRGS YRCNCNSGYE 800
PDASGRNCID IDECLVNRLL CDNGLCRNTP GSYSCTCPPG YVFRTETETC 850
EDINECESNP CVNGACRNNL GSFNCECSPG SKLSSTGLIC IDSLKGTCWL 900
NIQDSRCEVN INGATLKSEC CATLGAAWGS PCERCELDTA CPRGLARIKG 950
VTCEDVNECE VFPGVCPNGR CVNSKGSFHC ECPEGLTLDG TGRVCLDIRM 1000
EQCYLKWDED ECIHPVPGKF RMDACCCAVG AAWGTECEEC PKPGTKEYET 1050
LCPRGAGFAN RGDVLTGRPF YKDINECKAF PGMCTYGKCR NTIGSFKCRC 1100
NSGFALDMEE RNCTDIDECR ISPDLCGSGI CVNTPGSFEC ECFEGYESGF 1150
MMMKNCMDID ECERNPLLCR GGTCVNTEGS FQCDCPLGHE LSPSREDCVD 1200
INECSLSDNL CRNGKCVNMI GTYQCSCNPG YQATPDRQGC TDIDECMIMN 1250
GGCDTQCTNS EGSYECSCSE GYALMPDGRS CADIDECENN PDICDGGQCT 1300
NIPGEYRCLC YDGFMASMDM KTCIDVNECD LNSNICMFGE CENTKGSFIC 1350
HCQLGYSVKK GTTGCTDVDE CEIGAHNCDM HASCLNIPGS FKCSCREGWI 1400
GNGIKCIDLD ECSNGTHQCS INAQCVNTPG SYRCACSEGF TGDGFTCSDV 1450
DECAENINLC ENGQCLNVPG AYRCECEMGF TPASDSRSCQ DIDECSFQNI 1500
CVFGTCNNLP GMFHCICDDG YELDRTGGNC TDIDECADPI NCVNGLCVNT 1550
PGRYECNCPP DFQLNPTGVG CVDNRVGNCY LKFGPRGDGS LSCNTEIGVG 1600
VSRSSCCCSL GKAWGNPCET CPPVNSTEYY TLCPGGEGFR PNPITIILED 1650
IDECQELPGL CQGGNCINTF GSFQCECPQG YYLSEDTRIC EDIDECFAHP 1700
GVCGPGTCYN TLGNYTCICP PEYMQVNGGH NCMDMRKSFC YRSYNGTTCE 1750
NELPFNVTKR MCCCTYNVGK AWNKPCEPCP TPGTADFKTI CGNIPGFTFD 1800
IHTGKAVDID ECKEIPGICA NGVCINQIGS FRCECPTGFS YNDLLLVCED 1850
IDECSNGDNL CQRNADCINS PGSYRCECAA GFKLSPNGAC VDRNECLEIP 1900
NVCSHGLCVD LQGSYQCICH NGFKASQDQT MCMDVDECER HPCGNGTCKN 1950
TVGSYNCLCY PGFELTHNND CLDIDECSSF FGQVCRNGRC FNEIGSFKCL 2000
CNEGYELTPD GKNCIDTNEC VALPGSCSPG TCQNLEGSFR CICPPGYEVK 2050
SENCIDINEC DEDPNICLFG SCTNTPGGFQ CLCPPGFVLS DNGRRCFDTR 2100
QSFCFTNFEN GKCSVPKAFN TTKAKCCCSK MPGEGWGDPC ELCPKDDEVA 2150
FQDLCPYGHG TVPSLHDTRE DVNECLESPG ICSNGQCINT DGSFRCECPM 2200
GYNLDYTGVR CVDTDECSIG NPCGNGTCTN VIGSFECNCN EGFEPGPMMN 2250
CEDINECAQN PLLCAFRCMN TFGSYECTCP IGYALREDQK MCKDLDECAE 2300
GLHDCESRGM MCKNLIGTFM CICPPGMARR PDGEGCVDEN ECRTKPGICE 2350
NGRCVNIIGS YRCECNEGFQ SSSSGTECLD NRQGLCFAEV LQTICQMASS 2400
SRNLVTKSEC CCDGGRGWGH QCELCPLPGT AQYKKICPHG PGYTTDGRDI 2450
DECKVMPNLC TNGQCINTMG SFRCFCKVGY TTDISGTSCI DLDECSQSPK 2500
PCNYICKNTE GSYQCSCPRG YVLQEDGKTC KDLDECQTKQ HNCQFLCVNT 2550
LGGFTCKCPP GFTQHHTACI DNNECGSQPS LCGAKGICQN TPGSFSCECQ 2600
RGFSLDATGL NCEDVDECDG NHRCQHGCQN ILGGYRCGCP QGYIQHYQWN 2650
QCVDENECSN PNACGSASCY NTLGSYKCAC PSGFSFDQFS SACHDVNECS 2700
SSKNPCNYGC SNTEGGYLCG CPPGYYRVGQ GHCVSGMGFN KGQYLSLDTE 2750
VDEENALSPE ACYECKINGY SKKDSRQKRS IHEPDPTAVE QISLESVDMD 2800
SPVNMKFNLS HLGSKEHILE LRPAIQPLNN HIRYVISQGN DDSVFRIHQR 2850
NGLSYLHTAK KKLMPGTYTL EITSIPLYKK KELKKLEESN EDDYLLGELG 2900
EALRMRLQIQ LY 2912
Length:2,912
Mass (Da):314,775
Last modified:May 26, 2009 - v3
Checksum:i0F0D78319E9911E6
GO
Isoform 2 (identifier: P35556-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     113-145: Missing.
     1491-1506: DIDECSFQNICVFGTC → GGSPGFQLIFKLDQPQ
     1507-2912: Missing.

Show »
Length:1,473
Mass (Da):157,690
Checksum:i2B6620CFCA6F7A72
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti391 – 3911E → K in DA9.
VAR_015851
Natural varianti594 – 5941T → S.2 Publications
VAR_054979
Natural varianti681 – 6811R → H.1 Publication
VAR_054980
Natural varianti754 – 7541G → S in DA9. 1 Publication
VAR_058364
Natural varianti965 – 9651V → I.3 Publications
Corresponds to variant rs154001 [ dbSNP | Ensembl ].
VAR_002349
Natural varianti1057 – 10571G → D in DA9. 2 Publications
VAR_054981
Natural varianti1091 – 10911N → S in DA9. 1 Publication
VAR_058365
Natural varianti1093 – 10931I → T in DA9. 2 Publications
VAR_054982
Natural varianti1115 – 11151D → H in DA9; the underlying nucleotide substitution also causes low level in-frame mis-splicing of exon 25. 2 Publications
VAR_010739
Natural varianti1122 – 11221S → P in DA9. 1 Publication
VAR_058366
Natural varianti1142 – 11421C → F in DA9. 2 Publications
VAR_010740
Natural varianti1142 – 11421C → R in DA9. 1 Publication
VAR_058367
Natural varianti1146 – 11461Y → C in DA9. 1 Publication
VAR_058368
Natural varianti1156 – 11561C → F in DA9. 1 Publication
VAR_058369
Natural varianti1161 – 11611E → K in DA9. 1 Publication
VAR_058370
Natural varianti1179 – 11791G → C in DA9. 1 Publication
VAR_054983
Natural varianti1198 – 11981C → Y in DA9. 1 Publication
VAR_054984
Natural varianti1240 – 12401C → R in DA9. 1 Publication
VAR_054985
Natural varianti1246 – 12461C → F in DA9. 1 Publication
VAR_058371
Natural varianti1253 – 12531C → W in DA9. 2 Publications
Corresponds to variant rs28931602 [ dbSNP | Ensembl ].
VAR_010741
Natural varianti1253 – 12531C → Y in DA9. 2 Publications
VAR_002350
Natural varianti1257 – 12571C → W in DA9. 1 Publication
VAR_054986
Natural varianti1268 – 12681C → R in DA9. 1 Publication
VAR_054987
Natural varianti1384 – 13841C → F in DA9. 1 Publication
VAR_058372
Natural varianti1384 – 13841C → Y in DA9. 1 Publication
VAR_058373
Natural varianti1408 – 14081D → N in DA9. 1 Publication
VAR_058374
Natural varianti1425 – 14251C → R in DA9. 1 Publication
VAR_058375
Natural varianti1434 – 14341C → S in DA9. 2 Publications
VAR_002351
Natural varianti1772 – 17721W → G.2 Publications
VAR_054988
Natural varianti2062 – 20621E → V Found in a renal cell carcinoma case; somatic mutation. 1 Publication
VAR_064705
Natural varianti2266 – 22661F → L.2 Publications
VAR_054989
Natural varianti2278 – 22781T → M.
Corresponds to variant rs2307109 [ dbSNP | Ensembl ].
VAR_055415
Natural varianti2311 – 23111M → V.
Corresponds to variant rs32209 [ dbSNP | Ensembl ].
VAR_055416
Natural varianti2428 – 24281P → T.1 Publication
Corresponds to variant rs1801169 [ dbSNP | Ensembl ].
VAR_016143
Natural varianti2580 – 25801S → L.1 Publication
Corresponds to variant rs2291628 [ dbSNP | Ensembl ].
VAR_055417
Natural varianti2581 – 25811L → S.
Corresponds to variant rs2291628 [ dbSNP | Ensembl ].
VAR_054990
Natural varianti2771 – 27711S → P.2 Publications
Corresponds to variant rs1801170 [ dbSNP | Ensembl ].
VAR_014664

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei113 – 14533Missing in isoform 2. VSP_037369Add
BLAST
Alternative sequencei1491 – 150616DIDEC…VFGTC → GGSPGFQLIFKLDQPQ in isoform 2. VSP_037370Add
BLAST
Alternative sequencei1507 – 29121406Missing in isoform 2. VSP_037371Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti146 – 1461I → L in BAG62163. 1 Publication
Sequence conflicti192 – 1954GPNR → AQP in AAA18950. 1 Publication
Sequence conflicti243 – 2431I → T in AAA18950. 1 Publication
Sequence conflicti243 – 2431I → T in BAG62163. 1 Publication
Sequence conflicti1161 – 11611E → G in AAA18950. 1 Publication
Sequence conflicti1161 – 11611E → G in CAB56757. 1 Publication
Sequence conflicti1244 – 12441D → G in BAG62163. 1 Publication
Sequence conflicti1409 – 14091L → R in CAB56757. 1 Publication
Sequence conflicti1503 – 15031F → S in AAA18950. 1 Publication
Sequence conflicti2584 – 25841A → G in AAA18950. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U03272 mRNA. Translation: AAA18950.1.
AK300440 mRNA. Translation: BAG62163.1.
AC025169 Genomic DNA. No translation available.
AC034235 Genomic DNA. No translation available.
AC113387 Genomic DNA. No translation available.
X62009 mRNA. Translation: CAB56757.1.
AB209735 mRNA. Translation: BAD92972.1.
CCDSiCCDS34222.1. [P35556-1]
PIRiA54105.
RefSeqiNP_001990.2. NM_001999.3. [P35556-1]
UniGeneiHs.519294.

Genome annotation databases

EnsembliENST00000262464; ENSP00000262464; ENSG00000138829. [P35556-1]
ENST00000508053; ENSP00000424571; ENSG00000138829. [P35556-1]
GeneIDi2201.
KEGGihsa:2201.
UCSCiuc003kuu.3. human. [P35556-1]

Polymorphism databases

DMDMi238054385.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U03272 mRNA. Translation: AAA18950.1 .
AK300440 mRNA. Translation: BAG62163.1 .
AC025169 Genomic DNA. No translation available.
AC034235 Genomic DNA. No translation available.
AC113387 Genomic DNA. No translation available.
X62009 mRNA. Translation: CAB56757.1 .
AB209735 mRNA. Translation: BAD92972.1 .
CCDSi CCDS34222.1. [P35556-1 ]
PIRi A54105.
RefSeqi NP_001990.2. NM_001999.3. [P35556-1 ]
UniGenei Hs.519294.

3D structure databases

ProteinModelPortali P35556.
SMRi P35556. Positions 75-996, 1073-2330, 2338-2721.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108495. 7 interactions.
IntActi P35556. 3 interactions.
STRINGi 9606.ENSP00000262464.

PTM databases

PhosphoSitei P35556.

Polymorphism databases

DMDMi 238054385.

Proteomic databases

MaxQBi P35556.
PaxDbi P35556.
PRIDEi P35556.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000262464 ; ENSP00000262464 ; ENSG00000138829 . [P35556-1 ]
ENST00000508053 ; ENSP00000424571 ; ENSG00000138829 . [P35556-1 ]
GeneIDi 2201.
KEGGi hsa:2201.
UCSCi uc003kuu.3. human. [P35556-1 ]

Organism-specific databases

CTDi 2201.
GeneCardsi GC05M127621.
GeneReviewsi FBN2.
H-InvDB HIX0005141.
HIX0137461.
HGNCi HGNC:3604. FBN2.
HPAi CAB026401.
HPA012853.
MIMi 121050. phenotype.
612570. gene.
neXtProti NX_P35556.
Orphaneti 115. Congenital contractural arachnodactyly.
PharmGKBi PA28017.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG12793.
HOGENOMi HOG000231768.
HOVERGENi HBG005643.
InParanoidi P35556.
OMAi SGRNCID.
OrthoDBi EOG7RV9F6.
PhylomeDBi P35556.
TreeFami TF316849.

Enzyme and pathway databases

Reactomei REACT_118572. Degradation of the extracellular matrix.
REACT_150331. Molecules associated with elastic fibres.
REACT_150366. Elastic fibre formation.

Miscellaneous databases

GenomeRNAii 2201.
NextBioi 8895.
PROi P35556.
SOURCEi Search...

Gene expression databases

ArrayExpressi P35556.
Bgeei P35556.
CleanExi HS_FBN2.
Genevestigatori P35556.

Family and domain databases

Gene3Di 3.90.290.10. 9 hits.
InterProi IPR026823. cEGF.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR011398. FBN/EtMIC4.
IPR009030. Growth_fac_rcpt_N_dom.
IPR017878. TB_dom.
[Graphical view ]
PANTHERi PTHR24039. PTHR24039. 1 hit.
Pfami PF12662. cEGF. 1 hit.
PF07645. EGF_CA. 41 hits.
PF00683. TB. 9 hits.
[Graphical view ]
PIRSFi PIRSF036312. Fibrillin. 1 hit.
SMARTi SM00181. EGF. 3 hits.
SM00179. EGF_CA. 43 hits.
[Graphical view ]
SUPFAMi SSF57184. SSF57184. 13 hits.
SSF57581. SSF57581. 9 hits.
PROSITEi PS00010. ASX_HYDROXYL. 43 hits.
PS00022. EGF_1. 2 hits.
PS01186. EGF_2. 37 hits.
PS50026. EGF_3. 45 hits.
PS01187. EGF_CA. 43 hits.
PS51364. TB. 9 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Structure and expression of fibrillin-2, a novel microfibrillar component preferentially located in elastic matrices."
    Zhang H., Apfelroth S.D., Hu W., Davis E.C., Sanguineti C., Bonadio J., Mecham R.P., Ramirez F.
    J. Cell Biol. 124:855-863(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS SER-594; GLY-1772; LEU-2266; LEU-2580 AND PRO-2771.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Placenta.
  3. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Linkage of Marfan syndrome and a phenotypically related disorder to two different fibrillin genes."
    Lee B., Godfrey M., Vitale E., Hori H., Mattei M.-G., Sarfarazi M., Tsipouras P., Ramirez F., Hollister D.W.
    Nature 352:330-334(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 752-2912 (ISOFORM 2).
  5. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 937-2912 (ISOFORM 1).
    Tissue: Aortic endothelium.
  6. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1112.
    Tissue: Liver.
  7. "Fibrillin-2 (FBN2) mutations result in the Marfan-like disorder, congenital contractural arachnodactyly."
    Putnam E.A., Zhang H., Ramirez F., Milewicz D.M.
    Nat. Genet. 11:456-458(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS DA9 TYR-1253 AND SER-1434, VARIANT ILE-965.
  8. "Clustering of FBN2 mutations in patients with congenital contractural arachnodactyly indicates an important role of the domains encoded by exons 24 through 34 during human development."
    Park E.-S., Putnam E.A., Chitayat D., Child A., Milewicz D.M.
    Am. J. Med. Genet. 78:350-355(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS DA9 ASP-1057 AND THR-1093, VARIANTS SER-594; HIS-681; ILE-965; GLY-1772; LEU-2266; THR-2428 AND PRO-2771.
  9. "A single mutation that results in an Asp-to-His substitution and partial exon skipping in a family with congenital contractural arachnodactyly."
    Babcock D., Gasner C., Francke U., Maslen C.
    Hum. Genet. 103:22-28(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT DA9 HIS-1115.
  10. "Two novel fibrillin-2 mutations in congenital contractural arachnodactyly."
    Belleh S., Zhou G., Wang M., Der Kaloustian V.M., Pagon R.A., Godfrey M.
    Am. J. Med. Genet. 92:7-12(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS DA9 PHE-1142 AND TRP-1253.
  11. "Ten novel FBN2 mutations in congenital contractural arachnodactyly: delineation of the molecular pathogenesis and clinical phenotype."
    Gupta P.A., Putnam E.A., Carmical S.G., Kaitila I., Steinmann B., Child A., Danesino C., Metcalfe K., Berry S.A., Chen E., Delorme C.V., Thong M.-K., Ades L.C., Milewicz D.M.
    Hum. Mutat. 19:39-48(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS DA9 ASP-1057; THR-1093; PHE-1142; CYS-1179; TYR-1198; ARG-1240; TRP-1253; TYR-1253; TRP-1257; ARG-1268 AND SER-1434, VARIANT ILE-965.
  12. "Comprehensive clinical and molecular assessment of 32 probands with congenital contractural arachnodactyly: report of 14 novel mutations and review of the literature."
    Callewaert B.L., Loeys B.L., Ficcadenti A., Vermeer S., Landgren M., Kroes H.Y., Yaron Y., Pope M., Foulds N., Boute O., Galan F., Kingston H., Van der Aa N., Salcedo I., Swinkels M.E., Wallgren-Pettersson C., Gabrielli O., De Backer J., Coucke P.J., De Paepe A.M.
    Hum. Mutat. 30:334-341(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS DA9 SER-754; SER-1091; HIS-1115; PRO-1122; ARG-1142; CYS-1146; PHE-1156; LYS-1161; PHE-1246; PHE-1384; TYR-1384; ASN-1408 AND ARG-1425.
  13. Cited for: VARIANT VAL-2062.

Entry informationi

Entry nameiFBN2_HUMAN
AccessioniPrimary (citable) accession number: P35556
Secondary accession number(s): B4DU01, Q59ES6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: May 26, 2009
Last modified: September 3, 2014
This is version 156 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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